2PK9

Structure of the Pho85-Pho80 CDK-cyclin Complex of the Phosphate-responsive Signal Transduction Pathway

2PK9 の概要

• エントリーDOI: 10.2210/pdb2pk9/pdb
• 関連するPDBエントリー: 2PMI
• 分子名称: Cyclin-dependent protein kinase PHO85, PHO85 cyclin PHO80, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: cyclin-dependent kinase, cyclin, signaling protein, transferase- cell cycle complex, transferase-cell cycle complex, transferase/cell cycle
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139651.38

構造登録者

Huang, K.,Ferrin-O'Connell, I.,Zhang, W.,Leonard, G.A.,O'Shea, E.K.,Quiocho, F.A. (登録日: 2007-04-17, 公開日: 2007-12-11, 最終更新日: 2024-02-21)

主引用文献

Huang, K.,Ferrin-O'Connell, I.,Zhang, W.,Leonard, G.A.,O'Shea, E.K.,Quiocho, F.A.
Structure of the Pho85-Pho80 CDK-Cyclin Complex of the Phosphate-Responsive Signal Transduction Pathway
Mol.Cell, 28:614-623, 2007

PubMed Abstract: The ability to sense and respond appropriately to environmental changes is a primary requirement of all living organisms. In response to phosphate limitation, Saccharomyces cerevisiae induces transcription of a set of genes involved in the regulation of phosphate acquisition from the ambient environment. A signal transduction pathway (the PHO pathway) mediates this response, with Pho85-Pho80 playing a vital role. Here we report the X-ray structure of Pho85-Pho80, a prototypic structure of a CDK-cyclin complex functioning in transcriptional regulation in response to environmental changes. The structure revealed a specific salt link between a Pho85 arginine and a Pho80 aspartate that makes phosphorylation of the Pho85 activation loop dispensable and that maintains a Pho80 loop conformation for possible substrate recognition. It further showed two sites on the Pho80 cyclin for high-affinity binding of the transcription factor substrate (Pho4) and the CDK inhibitor (Pho81) that are markedly distant to each other and the active site.

PubMed: 18042456
DOI: 10.1016/j.molcel.2007.09.013

実験手法

X-RAY DIFFRACTION (2.906 Å)